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Asp3Gly polymorphism affects fatty acid‐binding protein 3 intracellular stability and subcellular localization
Author(s) -
Kusudo Tatsuya,
Hashida Yasuhiko,
Ando Fujiko,
Shimokata Hiroshi,
Yamashita Hitoshi
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.07.007
Subject(s) - intracellular , mutant , fatty acid binding protein , subcellular localization , fatty acid metabolism , metabolism , fatty acid , microbiology and biotechnology , biochemistry , amino acid , chemistry , function (biology) , mutation , biology , gene
Fatty acid‐binding proteins (FABP) play a crucial role in intracellular fatty acid transportation and metabolism. In this study, we investigate the effects of the FABP3 Asp3Gly (D3G) polymorphism on protein structure and function. Although the mutation did not alter protein secondary structure or the ability to bind 1‐anilinonaphthalene‐8‐sulfonic acid and palmitate, the intracellular stability of the D3G mutant was significantly decreased. Immunocytochemical analysis reveals that the mutation alters FABP3 subcellular localization. Our results suggest that the D3G polymorphism may impact energy metabolism and physiological functions.